STRUCTURE SOLUTION OF C-REACTIVE PROTEINS - MOLECULAR REPLACEMENT WITH A TWIST

Citation
Ak. Shrive et al., STRUCTURE SOLUTION OF C-REACTIVE PROTEINS - MOLECULAR REPLACEMENT WITH A TWIST, Acta crystallographica. Section D, Biological crystallography, 52, 1996, pp. 1049-1057
Citations number
26
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Crystallography,"Biochemical Research Methods",Biology
ISSN journal
0907-4449
Volume
52
Year of publication
1996
Part
6
Pages
1049 - 1057
Database
ISI
SICI code
0907-4449(1996)52:<1049:SSOCP->2.0.ZU;2-L
Abstract
The pentameric structure of C-reactive proteins (CRP) has been derived by a combination of automated and manual molecular-replacement techni ques. The method is generally applicable to other multimeric assemblie s. The highly homologous human serum amyloid P component (hSAP) struct ure fails to provide a pentameric molecular-replacement solution for C RP. In the absence of a significant signal from an individual protomer , the hSAP structure has been manually modified in terms of protomer a ssembly to provide the true pentameric model of CRP. The CRP protomers are rotated or twisted by 14 degrees about an axis, through the proto mer centre, which is approximately perpendicular to the pentamer radiu s and the molecular fivefold axis. The results demonstrate clearly tha t protomers with very similar folds arising from high sequence homolog y need not necessarily be assembled together in the same way although the symmetry of the resulting oligomer may be maintained. In a curious twist the CRP structure which provided the general CRP model remains unsolved, while the model itself has so far provided the solution of t wo other CRP structures.